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1. Erin Brender, MD, Writer; Alison Burke, MA, Illustrator; Richard M. Glass, MD (2005). Pancreatic cancer. Editor JAMA. 294:2934.

2. Ross MH, Reith EJ, Romrell LJ (1989). Histology: a text and atlas. 2nd ed.

Baltimore: Williams and Wilkins. 309-11.

3. Oertel JE, Heffess CS, Oertel YC (1992). Pancreas. In: Sternberg SS, ed. Histology for pathologists. 2nd ed. New York, NY: Raven Press. 652–68.

4. Dayal Y, O'Briain DS (1981). The pathology of the pancreatic endocrine cells. In:

Delellis RA, ed. Diagnostic immunohistochemistry (Masson monographs in diagnostic pathology). New York: Masson Publishing. 75-109.

5. Bordi C (1986). Endocrine pancreas. In: Spicer SS, ed. Histochemistry in athological diagnosis. Marcel Dekker, Inc, NewYork, Ch 16:457-79.

6. Cotran RS, Kumar V, Robbins SL (1989). Robbins pathologic basis of disease. 4th ed. Philadelphia: WB Saunders. 210–20.

7. Generoso U (2002). How far are we from the most accurate classification system for chronic Pancreatitis? JOP. J. Pancreas (Online) 3:62-65.

8. Chassin D, Benifla JL, Delattre C, Fernandez H, Ginisty D, Janneau JL, Prade M, Contesso G, Caillou B, Tournaire M, et. al. (1994). Identification of genes overexpressed in adenocarcinomas through preferential expression screening in trophoblasts. Cancer Res. 54:5217-23.

9. Vogelstein B, Kinzler KW (2004). Cancer genes and the pathways they control. Nat Med. 10:789–99.

10. Sanchez JA, Newman KD, Eichelberger MR et. al. (1990). The papillary-cystic neoplasm of the pancreas. Arch. Surgery 125:1502-5.

11. Warshaw AL, Compton CC, Lewandrowski K et. al. (1990). Cystic adeno-carcinomas of the pancreas: new clinical, radiologic and pathologic observations in 67 patients. Ann. Surgery. 212:432-43.

12. Lippincott JB Company (1992). Exocrine pancreas in: American Joint Committee on Cancer: Manual for Staging of Cancer. 4th ed. Philadelphia. 109-13.

13. Schumacher M et. al. (1986). Primary structure of Torpedo californic a cetylcholin-esterase deduced from its cDNA sequence. Nature 319:407–9.

14. Goding JW (2000). Ectoenzymes: physiology meets pathology. J. Leukoc. Biol.

67:285–311.

15. Sumitomo M, Shen R, Goldberg JS, Dai J, Navarro D and Nanus DM (2000).

Neutral endopeptidase promotes phorbol ester induced apoptosis in prostate cancer cells by inhibiting neuropeptide-induced protein kinase C delta degradation. Cancer Res. 60:6590-96.

16. Sumitomo M, Shen R, Walburg M, Dai J, Geng Y, Navarro D, et. al. (2000). Neutral endopeptidase inhibits prostate cancer cell migration by blocking focal adhesion kinase signaling. J. Clin. Invest. 106:1399-1407.

17. Lendeckel U, Kähne T, Riemann D, Neubert K, Arndt M and Reinhold D (2000). The role of membrane peptidases in immune functions (Review). Adv. Exp. Med. Biol.

477:1-24.

18. Van der Velden VHJ, Hulsmann AR (1999). Peptidases structure, function and modulation of peptide mediated effects in the human lung. Immunology. 29:445–56.

19. Shipp MA and Look T (1993). Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key. Blood 82:1052-70.

20. Shipp MA, Richardson NE, Sayre PH et. al. (1988). Molecular cloning of the common acute lymphoblastic leukaemia antigen (CALLA) identifies a type II integral membrane protein. Proc. Natl. Acad. Sci. 85:4819-23.

21. Letarte M, Vera S, Tran R, Addis JBL, Onizuka RJ, Quackenbush EJ, Jongneel CV, McInnes RR (1988). Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J. Exp. Med. 168:1247-53.

22. Malfroy B, Kuang WJ, Seeburg PH, Mason AJ and Schofield PR (1988) Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase).

FEBS Lett 229:206-10.

23. Riemann D (2002). CD10. In: Wiley Encyclopedia of Molecular Medicine. John Wiley

& Sons, Inc. 5:544-47.

24. Oefner C, D'Arcy A, Hennig M, Winkler FK and Dale GE (2000). Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon. J. Mol. Biol.

296:341-49.

25. Barker PE, Shipp MA, D'Adamio L, Masteller EL and Reinherz EL (1989). The common acute lymphoblastic leukemia antigen maps to chromosomal region 3 (q21-q27). J. Immunol. 142:283-87.

26. Tran-Paterson R, Willard HF and Letarte M (1989). The common acute lymphoblastic leukemia antigen (neutral endopeptidase-3.4.24.11.) gene is located on human chromosome 3. Cancer Genet. Cytogenet. 42:129-34.

27. Ishimaru F, Shipp MA (1995). Analysis of the human CD10/neutral endopeptidase 24.11 promoter region: two separate regulatory elements. Blood 85:3199–207.

28. Iijima H, Gerard NP, Squassoni C, Ewig J, Face D, Drazen JM et. al. (1992). Exon 16 del: a novel form of human neutral endopeptidase (CALLA). Am. J. Physiol.

262:725–29.

29. Lambert DM, Mergen F, Berens CF, Poupaert JH, Dumont P (1995). Synthesis and pharmacological properties of 2-[S-acetylthiorphan]-1,3- diacylaminopropan-2-ol derivatives as chimeric lipid drug carriers containing an enkephalinase inhibitor.

Pharm. Res. 12:187-91.

30. Hamza H, Khalifa HB, Baumer P, Berard H, Lecomte JM (1999). Racecadotril versus placebo in the treatment of acute diarrhoea in adults. Aliment. Pharmacol.

Ther. 13:15–19.

31. Lecomte JM (2000). An overview of clinical studies with racecadotril in adults. Int. J.

Antimicrob. Agents 14:81–87.

32. Prado D (2002). A multinational comparison of racecadotril and loperamide in the treatment of watery diarrhoea in adults. Scand. J. Gastroenterol. 37:656–61.

33. de Felipe MC, Jimenez I, Castro A, Fuentes JA (1989). Antidepressant action of imipramine and iprindole in mice is enhanced by inhibitors of enkephalin-degrading peptidases. Eur. J. Pharmacol. 159:175-80.

34. Wilkinson IB, McEniery CM, Bongaerts KH, MacCallum H, Webb DJ, Cockcroft JR (2001). Adrenomedullin (ADM) in the human forearm vascular bed: effect of neutral endopeptidase inhibition and comparison with proadrenomedullin NH2-terminal 20 peptide (PAMP). Br. J. Clin. Pharmacol. 52:159-64.

35. Ohbayashi H, Yamaki K, Suzuki R, Kume H, Takagi K (1998). Neutral endopeptidase 3.4.24.11 inhibition potentiates the inhibitory effects of type-C natriuretic peptide on leukotriene D4-induced airway changes. Clin. Exp. Pharmacol.

Physiol. 25:986-91.

36. de Gouw HW, Diamant Z, Kuijpers EA, Sont JK, Sterk PJ (1996). Role of neutral endopeptidase in exercise-induced bronchoconstriction in asthmatic subjects. J.

Appl. Physiol. 81:673-8.

37. Nichol GM, O'Connor BJ, Lecomte JM, Chung KF, Barnes PJ (1992). Effect of neutral endopeptidase inhibitor on airway function and bronchial responsiveness in asthmatic subjects. Eur. J. Clin. Pharmacol. 42:491-4.

38. Gilles Salles, Hans-Reimer Rodwald, Bridget S, Chin, Ellis L, Reinherz and Margaret A, Shipp (1993). Inhibition of CD10/neutral endopeptidase 24.11 promotes B-cell reconstitution and maturation in vivo. Immunology. 90:7618-22.

39. Ritz J, Pepsidero JM, Notis-McConary J, et. al. (1980, 1982). A monoclonal antibody to human acute lymphoblastic leukemia antigen. Nature 283:583-85, 76:4350-54.

40. Dowell BL, Borowitz MJ, Boyett JM, Pullen DJ, Crist WM, Quddus FF, Russell E C, Falletta JM, Metzgar RS (1987). Immunologic and clinicopathologic features of common acute lymphoblastic leukemia antigen-positive childhood T-cell leukemia. A Pediatric Oncology Group Study. Cancer. 59:2020-6.

41. Greaves MF, Hariri G, Newman RA, Sutherland DR, Ritter MA and Ritz J (1983).

Selective expression of the common acute lymphoblastic leukemia (gp 100) antigen on immature lymphoid cells and their malignant counterparts. Blood. 61:628-39.

42. Gregory CD, Tursz T, Edwards CF, Tetaud C, Talbot M, Caillou B, Rickinson A B and Lipinski M (1987). Identification of a subset lymphoma of normal B cells with a burkitt’s lymphoma (BL)-like phenotype. J. immunol. 139:313-18.

43. Harris NL, Bhan AK (1985). B-cell neoplasms of the lymphocytic, lympho-plasmacytoid and plasma cell types: immunohistologic analysis and clinical correlation. Hum. Pathol. 16:829-37.

44. Stein H, Lennert K, Feller AC, Mason DY (1984). Immunohistochemical analysis of human lymphoma: Correlation of histological and immunological categories. Adv.

Cancer Res. 42:67–147.

45. Weiss LM, Bindl JM, Picozzi VJ, Link MP and Warnke RA (1986). Lymphoblastic lymphoma: an immunophenotype study of 26 cases with comparison to T cell acute lymphoblastic leukaemia. Blood 67:474-78.

46. Plant JL, LeBien TW, Michael AF. Et. al. (1983). Stages of renal ontogenesis identified with monoclonal antibodies reactive with lymphohematopoietic differentiation antigens. J. Exp. Med. 157:155-72.

47. Metzger RS, Borowitz MJ, Jones NH, et. al. (1981). Distribution of common acute lymphoblastic leukemia antigen In nonhematopoietic tissues. J. Exp. Mcd.

154:1249-54.

48. Braun MP, Martin PJ, Ledbetter LA, et. al. (1983). Granulocytes and cultured human fibroblasts express common acute lymphoblastic antigen. Blood 61:718-25.

49. Carrel S, De Tribolet N, Gross N (1982). Expression of HLA-DR and common acute lymphoblastic leukemia antigen on glioma cells. Eur. J. Immunol. 12:354-57.

50. Carrel S, Schmidt-Kessen A, Mach JP, et. al. (1983). Expression of common acute lymphoblastic antigen [CALLA/ on human malignant melanoma cell lines. J.

Immunol.130:2456-60.

51. Seshadri R, Matthews C, Henerson DW, et. al. (1986). A human retino-blastoma cell line expressing the common acute lymphoblastic leukemia antigen and displaying an unusual chromosome abnormality. Cancer Genet. Cytogenet. 20:345-52.

52. Mechtersheimer G, Moiler P, (1989). Expression of the common acute lymphoblastic leukemia antigen (CD 10) in mesenchymal adenocarcinomas. Am. J. Pathol.

134:961-65.

53. Pesando JM, Tomaselli KJ, Lasarus H, et. al. (1983). Distribution and modulation of a human leukemia-associated antigen (CALLA). J. Immunol. 131:2038-45.

54. Howell S, Kenney J, Yurner AJ (1992). A survey of membrane peptidases in two human colonic cell lines. Caco-2 and HT-29. Biochem. J. 284:595-601.

55. Jalal F, Jumarie C, Bawab W, et. al. (1992). Polarized distribution of neutral endopeptidase 24.11 at the cell surface of cultured human intestinal epithelial Caco-2 cells. Biochem, J, Caco-288:945-51.

56. Chu P, Arber DA (2000). Paraffin-section detection of CD10 in 505 nonhematopoietic neoplasms. Frequent expression in renal cell adenocarcinoma and endometrial stromal sarcoma. Am. J. Clin. Pathol. 113:374-82.

57. Langner C, Ratschek M, Rehak P, et. al. (2004). CD10 is a diagnostic and prognostic marker in renal malignancies. Histopathology 45:460-7.

58. Koiso K, Akaza H, Ohtani M, et. al. (1994). A new adenocarcinoma marker for bladder cancer. Int. J. Urol. 1:33 -6.

59. Tawfic S, Niehans GA, Manivel JC (2003). The pattern of CD10 expression in selected pathologic entities of the prostate gland. Hum. Pathol. 34:450-6.

60. Ordi J, Romagosa C, Tavassoli FA, et. al. (2003). A CD10 expression in epithelial tissues and adenocarcinomas of the gynecologic tract: a useful marker in the diagnosis of mesonephric, trophoblastic and clear cell adenocarcinomas. Am. J.

Surg. Pathol. 27:178-86.

61. Shousha S, Gadir F, Peston D, et. al. (2004). CD10 immunostaining of bile canaliculi in liver biopsies: change of staining pattern with the development of cirrhosis. Histopathology 45:335-42.

62. Khin EE, Kikkawa F, Ino K, et. al. (2003). NEP/CD10 expression in the stroma of epithelial ovarian adenocarcinoma. Int. J. Gynecol. Pathol. 22:175-80.

63. Ogawa H, Iwaya K, Izumi M, et. al. (2002). Expression of CD10 by stromal cells during colorectal adenocarcinoma development. Hum. Pathol. 33:806 -11.

64. Notohara K, Hamazaki S, Tsukayama C, et. al. (2000). Solid-pseudopapillary adenocarcinoma of the pancreas: immunohistochemical localization of neuroendocrine markers and CD10. Am. J. Surg. Pathol. 24:1361-71.

65. Jorge Albores-Saavedra, MD, Karen W. Simpson, MD and Seth J. Bilello, MD (2006). The clear cell variant of solid pseudopapillary adenocarcinoma of the pancreas: A previously unrecognized pancreatic neoplasm. Am. J. Surg. Pathol.

30:1237–42.

66. Chen C, Jing W, Gulati P, Vargas H, French SW (2004). Melanocytic differentiation in a solid pseudopapillary adenocarcinoma of the pancreas. J Gastroenterol.

39:579-83.

67. Lydia Deschamps MD, Adriana Handra-Luca MD, PhD, Dermot O’Toole MD, PhD, Alain Sauvanet MD, Philippe Ruszniewski MD, Jacques Belghiti MD, Pierre Bedossa MD, PhD, Anne Couvelard MD, PhD (2006). CD10 expression in pancreatic endocrine adenocarcinomas: correlation with prognostic factors and survival. Human Pathology 37:802–8.

68. Broccolini A, Gidaro T, Morosetti R, Gliubizzi C, Servidei T, Pescatori M, Tonali PA, Ricci E, Mirabella M (2006). Neprilysin participates in skeletal muscle regeneration and is accumulated in abnormal muscle fibres of inclusion body myositis. J.

Neurochem. 96:777-89.

69. Fielitz J, Dendorfer A, Pregla R, Ehler E, Zurbrugg HR, Bartunek J, Hetzer R, Regitz-Zagrosek V (2002). Neutral endopeptidase is activated in cardiomyocytes in human aortic valve stenosis and heart failure. Circulation. 105:286-9.

70. Olerud JE, Usui ML, Seckin D, Chiu DS, Haycox CL, Song IS, Ansel JC, Bunnett NW (1999). Neutral endopeptidase expression and distribution in human skin and wounds. J. Invest. Dermatol. 112:873-81.

71. Guerin S, Mari B, Maulon L, Belhacene N, Marguet D, Auberger P (1997). CD10 plays a specific role in early thymic development. FASEB J. 11:376-81.

72. Baraniuk JN, Ohkubo K, Kwon OJ, Mak J, Ali M, Davies R, Twort C, Kaliner M, Letarte M, Barnes PJ (1995). Localization of neutral endopeptidase (NEP) mRNA in human bronchi. Eur. Respir. J. 8:1458-64.

73. Mari B, Breittmayer JP, Guerin S, Belhacene N, Peyron JF, Deckert M, Rossi B, Auberger P (1994). High levels of functional endopeptidase 24.11 (CD10) activity on human thymocytes: preferential expression on immature subsets. Immunology.

82:433-8.

74. Skryzdlo-Radomanska B, Pollard H, Schabowski J, Radwan P, Celinski K, Pokora J, Gespach C (1994). [Activity of enkephalinase (EC.3.4.24.11). Neutral endopeptidase in human digestive tract epithelial cells]. Wiad. Lek. 47:13-7.

75. Ohkubo K, Baraniuk JN, Hohman RJ, Kaulbach HC, Hausfeld JN, Merida M, Kaliner MA (1993). Human nasal mucosal neutral endopeptidase (NEP): location, quantitation and secretion. Am J Respir Cell Mol Biol. 9:557-67.

76. Salles G, Rodewald HR, Chin BS, Reinherz EL, Shipp MA (1993). Inhibition of CD10/neutral endopeptidase 24.11 promotes B-cell reconstitution and maturation in vivo. Proc. Natl. Acad. Sci. U S A. 90:7618-22.

77. Wen-Bin Huang, Xiao-Jun Zhou, Jie-Yu Chen, Li-Hua Zhang, Kui Meng, Heng-Hui Ma and Zhen-Feng Lu (2005). CD10-positive Stromal Cells in Gastric Adenocarcinoma: Correlation with Invasion and Metastasis. Jpn. J. Clin. Oncol.

35:245-50.

78. Nurija Bilalovic, Berit Sandstad, Rastko Golouh, Jahn M Nesland, Ivan Selak and Emina E Torlakovic (2004). CD10 protein expression in adenocarcinoma and stromal cells of malignant melanoma is associated with adenocarcinoma progression. Modern Pathology 17:1251–58.

79. Khin EE, Kikkawa F, Ino K, Suzuki T, Shibata K, Kajiyama H, Tamakoshi K, Mizutani S (2003). Neutral endopeptidase/CD10 expression in the stroma of epithelial ovarian adenocarcinoma. Int. J. Gynecol. Pathol. 22:175-80.

80. Kajiyama H, Shibata K, Terauchi M, Morita T, Ino K, Mizutani S, Kikkawa F (2005).

Neutral endopeptidase 24.11/CD10 suppresses progressive potential in ovarian adenocarcinoma in vitro and in vivo. Clin. Cancer Res. 11:1798-808.

81. Ogawa H, Iwaya K, Izumi M, Kuroda M, Serizawa H, Koyanagi Y, Mukai K (2002).

Expression of CD10 by stromal cells during colorectal adenocarcinoma development. Hum. Pathol. 33:806-11.

82. Uehara C, Ino K, Suzuki T, Kajiyama H, Kikkawa F, Nagasaka T, Mizutani S (2001).

Upregulation of Neutral endopeptidase expression and enzymatic activity during the differentiation of human chorioadenocarcinoma cells. Placenta. 22:540-9.

83. Mazur-Kolecka B, Frackowiak J (2006). Neprilysin protects human neuronal progenitor cells against impaired development caused by amyloid-beta peptide.

Brain Res. 1124:10-8.

84. Poirier R, Wolfer DP, Welzl H, Tracy J, Galsworthy MJ, Nitsch RM, Mohajeri MH (2006). Neuronal neprilysin over expression is associated with attenuation of Abeta-related spatial memory deficit. Neurobiol. Dis. 24:475-83.

85. Bircan S, Candir O, Kapucuoglu N, Serel TA, Ciris M, Karahan N (2006). CD10 expression in urothelial bladder adenocarcinomas: a pilot study. Urol Int. 77:107-13.

86. Braham H, Trimeche M, Ziadi S, Mestiri S, Mokni M, Amara K, Hachana M, Sriha B, Korbi S (2006). CD10 expression by fusiform stromal cells in nasopharyngeal adenocarcinoma correlates with adenocarcinoma progression. Virchows Arch.

449:220-4.

87. Terauchi M, Kajiyama H, Shibata K, Ino K, Mizutani S, Kikkawa F (2005). Anti-progressive effect of Neutral endopeptidase 24.11 (NEP/CD10) on cervical adenocarcinoma in vitro and in vivo. Oncology. 69:52-62.

88. Piattelli A, Fioroni M, Iezzi G, Perrotti V, Stellini E, Piattelli M, Rubini C (2006). CD10 expression in stromal cells of oral cavity squamous cell adenocarcinoma: a clinic and pathologic correlation. Oral Dis. 12:301-4.

89. Erhuma M, Kobel M, Mustafa T, Wulfanger J, Dralle H, Hoang-Vu C, Langner J, Seliger B, Kehlen A (2007). Expression of Neutral endopeptidase (NEP/CD10) on pancreatic tumor cell lines, pancreatitis and pancreatic tumor tissues. Int. J. Cancer 120:2393-400.

90. Chomczynski P, Sacchi N (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 162:156-9.

91. Mosmann T (1983). Rapid colorimetric assay for cellular growth and survival:

application to proliferation and cytotoxicity assays. J. Immunol. Methods. 65:55-63.

92. Mari B, Checler F, Ponzio G, Peyron JF, Manie S, Farahifar D, Rossi B and Auberger P (1992). Jurkat T cells express a functional Neutral endopeptidase activity (CALLA) involved in T cell activation. EMBO J. 11: 3875-85.

93. Gabrilovac J, Cupic B, Breljak D, Zekusic M and Boranic M (2004). Expression of CD13/aminopeptidase N and CD10/Neutral endopeptidase on cultured human keratinocytes. Immunol. Lett. 91:39-47.

94. Aprikian AG, Tremblay L, Han K and Chevalier S (1997). Bombesin stimulates the motility of human prostate-adenocarcinoma cells through tyrosine phosphorylation of focal adhesion kinase and of integrin-associated proteins. Int. J. Cancer. 72:498–

504.

95. Elsasser HP, Lehr U, Agricola B, Kern HF (1992). Establishment and characterisation of two cell lines with different grade of differentiation derived from one primary human pancreatic adenocarcinoma. Virchows Arch B Cell Pathol. Incl.

Mol. Pathol. 61:295–306.

96. Nishimura N, Saito S, Kubota Y, Moto-o N, Taguchi K, Yamazaki K, Watanabe A, Sasaki H (1993). Newly established human pancreatic carcinoma cell lines and their lectin binding properties. Int. J. Pancreatol. 13:31-41.

97. Kyriazis AA, Kyriazis AP, Sternberg CN, Sloane NH, Loveless JD (1986).

Morphological, biological, biochemical and karyotypic characteristics of human pancreatic ductal adenocarcinoma Capan-2 in tissue culture and the nude mouse.

Cancer Res. 46:5810-5.

98. Michael Lieber, Joann Mazzetta, Walter Nelson-Rees, Michael Kaplan, George Todaro (1975). Establishment of a continuous tumor-cell line (PANC-1) from a human carcinoma of the exocrine pancreas. Int. J. of Cancer 15:741-47.

99. Tsutsumi S, Kuwano H, Morinaga N, Shimura T, Asao T (2001). Animal model of para-aortic lymph node metastasis. Cancer Letters 169:77-85.

100. Elsasser HP, Lehr U, Agricola B, Kern HF (1993). Structural analysis of a new highly metastatic cell line PA-TU-8902 from a primary human pancreatic adenocarcinoma.

Virchows Arch B Cell Pathol. Incl. Mol. Pathol. 64:201-7.

101. D'Adamio L, Shipp MA, Masteller EL, Reinherz EL (1989). Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5' untranslated regions. Proc. Natl. Acad.

Sci. USA 86:7103-7.

102. Ishimaru F, Mari B, Shipp MA (1997). The type 2 CD10/neutral endopeptidase 24.11 promoter: functional characterization and tissue-specific regulation by CBF/NF-Y isoforms. Blood 89:4136-45.

103. Badar A, Usmani, Ruoqian Shen, Michael Janeczko, Christos N, Papandreou, Wen-Hsiang Lee, William G, Nelson, Joel B, Nelson and David M, Nanus (2000).

Methylation of the Neutral Endopeptidase Gene Promoter in Human Prostate Cancers. Clinical Cancer Research 1664:1664–70.

104. Ganju RK, Sunday M, Tsarwhas DG, Card A and Shipp MA (1994). NEP/CD10 in non-small cell lung carcinomas. Relationship to cellular proliferation. J. Clin. Invest.

94:1784–91.

105. Shipp MA, George ET, Chang-Yan Chen, Stephanie NS, Louis BH, Harald S, Mary ES, Ellis LR (1991). CD10/Neutral Endopeptidase 24.11 Hydrolyzes Bombesin-Like Peptides and Regulates the Growth of Small Cell Carcinomas of the Lung. PNAS 88:10662-66.

106. Mikio Terauchi, Hiroaki Kajiyama, Kiyosumi Shibata, Kazuhiko Ino, Shigehiko Mizutani, Fumitaka Kikkawa (2005). Anti-Progressive Effect of Neutral Endopeptidase 24.11 (NEP/CD10) on Cervical Carcinoma in vitro and in vivo.

Oncology 69:52-62.

107. Lapadula G, Iannone F, Zuccaro C, Covelli M, Patella V, Lobianco G, Pipitone V (1995). Expression of membrane-bound peptidases (CD10 and CD26) on human articular chondrocytes. Possible role of neuropeptidases in the pathogenesis of osteoarthritis. Clin Exp Rheumatol.13:143-8.

108. Iwase A, Shen R, Navarro D, Nanus DM (2004). Direct binding of neutral endopeptidase 24.11 to ezrin/radixin/moesin (ERM) proteins competes with the interaction of CD44 with ERM proteins. J. Biol. Chem. 279:11898-905.

109. Sumitomo M, Milowsky MI, Shen R, Navarro D, Dai J, Asano T, Hayakawa M, Nanus DM (2001). Neutral endopeptidase inhibits neuropeptide-mediated transactivation of the insulin-like growth factor receptor Akt cell survival pathway.

Cancer Res. 61:3294-8.

110. Sumitomo M, Iwase A, Zheng R, Navarro D, Kaminetzky D, Shen R, Georgescu MM, Nanus DM (2004). Synergy in tumor suppression by direct interaction of neutral endopeptidase with PTEN. Cancer Cell 5:67-78.

111. Hofman P, Selva E, Le Negrate G, d'Andrea L, Guérin S, Rossi B, Auberger P (1998). CD10 inhibitors increase f-Met-Leu-Phe-induced neutrophil transmigration.

J. Leukoc. Biol. 63:312-20.

112. Rudland PS, Platt-Higgins A, Renshaw C, West CR, Winstanley JH, Robertson L, Barraclough R (2000). Prognostic significance of the metastasis-inducing protein S100A4 (p9Ka) in human breast cancer. Cancer Res. 60:1595–1603.

113. Mazzucchelli L (2002). Protein S100A4: too long overlooked by pathologists? Am. J.

Pathol. 160:7–13.

114. Cho YG, Nam SW, Kim TY, Kim YS, Kim CJ, Park JY, Lee JH, Kim HS, Lee JW, Park CH, Song YH, Lee SH, Yoo NJ, Lee JY, Park WS (2003). Over expression of S100A4 is closely related to the aggressiveness of gastric cancer. APMIS 111:539–

45.

115. Heman R, Fasheh R, Calabrese C, Frank AJ, Maclean KH, Allard D, Barraclough R, Gilbertson RJ (2003). ERBB2 up-regulates S100A4 and several other prometastatic genes in medulloblastoma. Cancer Res. 63:140–8.

116. Cui JF, Liu YK, Pan BS, Song HY, Zhang Y, Sun RX, Chen J, Feng JT, Tang ZY, Yu YL, Shen HL, Yang PY (2004). Differential pmteomic analysis of human hepatocellular carcinoma cell line metastasis-associated proteins. J. Cancer Res.

Clin. Oncol. 130: 615–22.

117. Missiaglia E, Blaveri E, Terris B, Wang YH, Costello E, Neoptolemos JP, Crnogorac-Jurcevic T, Lemoine NR (2004). Analysis of gene expression in cancer cell lines identifies candidate markers for pancreatic tumorigenesis and metastasis. Int. J.

Cancer 112:100–112.

118. Kriajevska MV, Cardenas MN, Grigorian MS, Ambartsumian NS, Georgiev GP, Lukanidin EM (1994). Non-muscle myosin heavy chain as a possible target for protein encoded by metastasis-related mts-1 gene. J. Biol. Chem. 269:19679–82.

119. Takenaga K, Nakamura Y, Endo H, Sakiyama S (1994a). Involvement of S100-related calcium-binding protein pEL98 (or mts 1) in cell motility and tumor cell invasion. Jpn. J. Cancer Res. 85:831–39.

120. Van Aelst L, D’Souza-Schorey C (1997). Rho GTPases and signalling networks.

Genes Dev. 11:2295–322.

121. Aznar S, Lacal JC (2001). Rho signals to cell growth and apoptosis. Cancer Lett.

165:1–10.

122. Aznar S, Lacal JC (2001). Searching new targets for anticancer drug design: the families of Ras, Rho GTPases and their effectors. Prog. Nucleic Acid Res. Mol. Biol.

67:193–234.

123. Schmitz AA, Govek EE, Bottner B, Van Aelst L (2000). Rho GTPases: signaling, migration and invasion. Exp. Cell Res. 261:1–12.

124. Jiang WG, Watkins G, Lane J, Cunnick GH, Douglas-Jones A, et. al. (2003).

Prognostic value of rho GTPases and rho guanine nucleotide dissociation inhibitors in human breast cancers. Clin. Cancer Res. 9:6432–40.

125. Fritz G, Brachetti C, Bahlmann F, Schmidt M, Kaina B (2002). Rho GTPases in human breast tumors: expression and mutation analyses and correlation with clinical parameters. Br. J. Cancer 87:635–44.

126. Fritz G, Just I, Kaina B (1999). Rho GTPases are over-expressed in human tumors.

Int. J. Cancer 81:682–87.

127. Eisenmann KM, McCarthy JB, Simpson MA, Keely PJ, Guan JL, et. al. (1999).

Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Nat. Cell Biol. 1:507–13.

128. Lawrenson ID, Wimmer-Kleikamp SH, Lock P, Schoenwaelder SM, Down M, et. al.

(2002). Ephrin-A5 induces rounding, blebbing and deadhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling. J. Cell Sci.

115:1059–72.

129. Attoub S, Noe V, Pirola L, Bruyneel E, Chastre E, et. al. (2000). Leptin promotes invasiveness of kidney and colonic epithelial cells via phosphoinositide 3-kinase-, rho- and rac-dependent signaling pathways. Faseb. J. 14:2329–38.

130. Varker KA, Phelps SH, King MM, Williams CL (2003). The small GTPase RhoA has greater expression in small cell lung carcinoma than in nonsmall cell lung carcinoma and contributes to their unique morphologies. Int. J. Oncol. 22:671–81.

131. Kamai T, Yamanishi T, Shirataki H, Takagi K, Asami H, et. al. (2004). Over expression of RhoA, Rac1 and Cdc42 GTPases is associated with progression in testicular cancer. Clin. Cancer Res. 10:4799–4805.

132. Takamura M, Sakamoto M, Genda T, Ichida T, Asakura H, et. al. (2001). Inhibition of intrahepatic metastasis of human hepatocellular carcinoma by Rho-associated protein kinase inhibitor Y-27632. Hepatology 33:577–81.

133. Mira JP, Benard V, Groffen J, Sanders LC, Knaus UG. (2000). Endogenous, hyperactive Rac3 controls proliferation of breast cancer cells by a p21-activated kinase-dependent pathway. PNAS 97:185–89.

134. Kawasaki Y, Sato R, Akiyama T. (2003). Mutated APC and Asef are involved in the migration of colorectal tumor cells. Nat. Cell Biol. 5:211–15.

135. Jung ID, Lee J, Yun SY, Park CG, Choi WS, et. al. (2002). Cdc42 and Rac1 are necessary for autotaxin-induced tumor cell motility in A2058 melanoma cells. FEBS Lett. 532:351–56.

136. Shieh DB, Godleski J, Herndon JE 2nd, Azuma T, Mercer H, et. al. (1999). Cell motility as a prognostic factor in Stage I nonsmall cell lung carcinoma: the role of gelsolin expression. Cancer 85:47–57.

137. Bouzahzah B, Albanese C, Ahmed F, Pixley F, Lisanti MP, et. al. (2001). Rho family GTPases regulate mammary epithelium cell growth and metastasis through distinguishable pathways. Mol. Med. 7:816–30.

138. Eisenmann KM, McCarthy JB, Simpson MA, Keely PJ, Guan JL, et. al. (1999).

Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Nat. Cell Biol. 1:507–13.

139. Abraham MT, Kuriakose MA, Sacks PG, Yee H, Chiriboga L, et. al. (2001). Motility-related proteins as markers for head and neck squamous cell cancer. Laryngoscope 111:1285-89.

140. Brattsand G, Roos G, Marklund U, Ueda H, Landberg G, Nanberg R, Sideras P and Gullberg M (1993). Quantitative analysis of the expression and regulation of an activation-regulated phosphoprotein (oncoprotein 18) in normal and neoplastic cells.

Leukemia 7:569-79.

141. Ghosh PK anderson J, Cohen N, Takeshita K, Atweh GF and Lebowitz P(1993).

Expression of the leukemia-associated gene, p18, in normal and malignant tissues;

inactivation of expression in a patient with cleaved B cell lymphoma/leukemia.

Oncogene 8:2869-72.

142. Jeha S, Luo XN, Beran M, Kantarijan H and Atweh GF (1996). Antisense RNA inhibition of phosphoprotein p18 expression abrogates the transformed phenotype of leukemic cells. Cancer Res. 56:1445-50.

143. Sobel A (1991). Stathmin: a relay phosphoprotein for multiple signal transduction?.

Trends Biochem. Sci. 16:301-6.